Bio-Organic Chemistry – Protein labeling
Institute for Chemistry and Biochemistry
Chemical modification of proteins is one of the most powerful biochemical tools for the study of protein structure and function. Cysteine is one of the most rarely used amino acids in proteins but often plays a crucial role by forming covalent disulfide bonds, coordinating metal ions, or mediating redox properties. Recently, our group has developed a new class of thiol-reactive reagents for protein derivatization.
Projects could include the study of their reactivity, selectivity, and applicability for analytical purposes, e.g. for fluorescent labeling of model compounds, proteins, and cells by using various methods of spectroscopy, chromatography, and electrophoresis.
Pre-requisites or requirements for the project
chemistry lab experience mandatory, preferentially organic synthesis and biochemistry lab
Literature and preparation
- textbooks in biochemistry
- H.-Y. Shiu et al. Chem. Eur. J. 2009, 15, 3839-3850
until end of March 2019